FabI

• Description: enoyl-acyl carrier protein reductase
  
  

Gene name	fabI
Synonyms	yjbW
Essential	no
Product	enoyl-acyl carrier protein reductase
Function	fatty acid biosynthesis
Gene expression levels in SubtiExpress: fabI
Metabolic function and regulation of this protein in SubtiPathways: fabI
MW, pI	27 kDa, 5.605
Gene length, protein length	774 bp, 258 aa
Immediate neighbours	thiD, cotO
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis of lipids

This gene is a member of the following regulons

FapR regulon

The gene

Basic information

• Locus tag: BSU11720

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Acyl-[acyl-carrier-protein] + NAD⁺ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH (according to Swiss-Prot)

• Protein family: FabI subfamily (according to Swiss-Prot)

• Paralogous protein(s): FabL, one of the two proteins has to be present for viability PubMed

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:
  • inhibited by triclosan PubMed

• Interactions:

• Localization:

Database entries

• Structure: 3OIF (complex with NAD and inhibitor triclosan) PubMed

• UniProt: P54616

• KEGG entry: [3]

• E.C. number: 1.3.1.9

Expression and regulation

• Operon: fabI PubMed

• Expression browser: fabI PubMed

• Sigma factor:

• Regulation:
  • expressed when the cells experience a lack of malonyl-CoA (FapR) PubMed
  • induced upon fatty acid biosynthesis inhibition PubMed

• Regulatory mechanism:
  • FapR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Yasutaro Fujita, Hiroshi Matsuoka, Kazutake Hirooka
Regulation of fatty acid metabolism in bacteria.
Mol Microbiol: 2007, 66(4);829-39
[PubMed:17919287] [WorldCat.org] [DOI] (P p)

Stephen W White, Jie Zheng, Yong-Mei Zhang, Rock
The structural biology of type II fatty acid biosynthesis.
Annu Rev Biochem: 2005, 74;791-831
[PubMed:15952903] [WorldCat.org] [DOI] (P p)

Original Publications

Michaela Wenzel, Malay Patra, Dirk Albrecht, David Y-K Chen, K C Nicolaou, Nils Metzler-Nolte, Julia E Bandow
Proteomic signature of fatty acid biosynthesis inhibition available for in vivo mechanism-of-action studies.
Antimicrob Agents Chemother: 2011, 55(6);2590-6
[PubMed:21383089] [WorldCat.org] [DOI] (I p)

Kook-Han Kim, Byung Hak Ha, Su Jin Kim, Seung Kon Hong, Kwang Yeon Hwang, Eunice Eunkyeong Kim
Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis.
J Mol Biol: 2011, 406(3);403-15
[PubMed:21185310] [WorldCat.org] [DOI] (I p)

Helena B Thomaides, Ella J Davison, Lisa Burston, Hazel Johnson, David R Brown, Alison C Hunt, Jeffery Errington, Lloyd Czaplewski
Essential bacterial functions encoded by gene pairs.
J Bacteriol: 2007, 189(2);591-602
[PubMed:17114254] [WorldCat.org] [DOI] (P p)

Gustavo E Schujman, Luciana Paoletti, Alan D Grossman, Diego de Mendoza
FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis.
Dev Cell: 2003, 4(5);663-72
[PubMed:12737802] [WorldCat.org] [DOI] (P p)

R J Heath, N Su, C K Murphy, C O Rock
The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis.
J Biol Chem: 2000, 275(51);40128-33
[PubMed:11007778] [WorldCat.org] [DOI] (P p)

C Baldock, J B Rafferty, S E Sedelnikova, P J Baker, A R Stuitje, A R Slabas, T R Hawkes, D W Rice
A mechanism of drug action revealed by structural studies of enoyl reductase.
Science: 1996, 274(5295);2107-10
[PubMed:8953047] [WorldCat.org] [DOI] (P p)